[Decreased collagen stability as a response to the loss of structural integrity of thyroid cartilage].
The thermal behavior, birefringence properties, and the biochemical composition of thyroid cartilage tissues have been studied. The hyaline cartilage, which was visualized as a quasi-isotropic medium, was composed of type II collagen, which did not denature at temperatures up to 100 degrees C. However, in hyaline cartilage digested by trypsin, the denaturation of collagen occured at 60 degrees C. Collagen fibers in the perichondrium were composed of type I and II collagen and formed a highly organized anisotropic structure (birefringence about 4.75 x 10(-3)) with a melting temperature of about 65 degrees C. The temperature of collagen denaturation in perichondrium in the whole system perichondrium-hyaline cartilage increased up to 75 degrees C, indicating the immobilization of perichondrium collagen by the extracellular matrix of the hyaline constituent.
Logunova
M A
MA
Shakhova
M A
MA
Andreeva
I V
IV
Ignat'eva
N Iu
NIu
Kanenskiĭ
V A
VA
Bagratashvili
V N
VN
D000818:Animals; D016880:Anisotropy; D002417:Cattle; D024042:Collagen Type I / Q000737:chemistry*; D024043:Collagen Type II / Q000737:chemistry*; D006358:Hot Temperature; D013957:Thyroid Cartilage / Q000737:chemistry*; D014357:Trypsin / Q000737:chemistry*
D024042:Collagen Type I; D024043:Collagen Type II; D014357:Trypsin